2jng: Difference between revisions
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New page: left|200px<br /> <applet load="2jng" size="450" color="white" frame="true" align="right" spinBox="true" caption="2jng" /> '''Solution structure of the CUL7-CPH domain f... |
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[[Image:2jng.gif|left|200px]]<br /> | [[Image:2jng.gif|left|200px]]<br /><applet load="2jng" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.'''<br /> | '''Solution structure of the CUL7-CPH domain from Homo Sapiens; Northeast Structural Genomics Consortium target HT1.'''<br /> | ||
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==Overview== | ==Overview== | ||
Cul7 is a member of the Cullin Ring Ligase (CRL) family and is required, for normal mouse development and cellular proliferation. Recently, a, region of Cul7 that is highly conserved in the p-53 associated, Parkin-like cytoplasmic protein, PARC, was shown to bind p53 directly., Here we identify the CPH domain (conserved domain within Cul7, PARC and, HERC2 proteins) of both Cul7 and PARC as a p53 interaction domain using, size exclusion chromatography and NMR spectroscopy. We present the first, structure of the evolutionary conserved CPH domain and provide novel, insight into the Cul7-p53 interaction. The NMR structure of the Cul7-CPH, domain reveals a fold similar to peptide interaction modules such as the, SH3, Tudor and KOW domains. The p53 interaction surface of both Cul7 and, PARC CPH domains was mapped to a conserved surface distinct from the, analogous peptide binding regions of SH3, KOW and Tudor domains, suggesting a novel mode of interaction. The CPH domain interaction surface, of p53 resides in the tetramerization domain and is formed by residues, contributed by at least two subunits. | Cul7 is a member of the Cullin Ring Ligase (CRL) family and is required, for normal mouse development and cellular proliferation. Recently, a, region of Cul7 that is highly conserved in the p-53 associated, Parkin-like cytoplasmic protein, PARC, was shown to bind p53 directly., Here we identify the CPH domain (conserved domain within Cul7, PARC and, HERC2 proteins) of both Cul7 and PARC as a p53 interaction domain using, size exclusion chromatography and NMR spectroscopy. We present the first, structure of the evolutionary conserved CPH domain and provide novel, insight into the Cul7-p53 interaction. The NMR structure of the Cul7-CPH, domain reveals a fold similar to peptide interaction modules such as the, SH3, Tudor and KOW domains. The p53 interaction surface of both Cul7 and, PARC CPH domains was mapped to a conserved surface distinct from the, analogous peptide binding regions of SH3, KOW and Tudor domains, suggesting a novel mode of interaction. The CPH domain interaction surface, of p53 resides in the tetramerization domain and is formed by residues, contributed by at least two subunits. | ||
==About this Structure== | ==About this Structure== | ||
2JNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2JNG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JNG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:19:00 2008'' | ||
